scholarly journals N-terminal and Central Segments of the Type 1 Ryanodine Receptor Mediate Its Interaction with FK506-binding Proteins

2013 ◽  
Vol 288 (22) ◽  
pp. 16073-16084 ◽  
Author(s):  
Tanya Girgenrath ◽  
Mohana Mahalingam ◽  
Bengt Svensson ◽  
Florentin R. Nitu ◽  
Razvan L. Cornea ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Binding Proteins ◽  
Fk506 Binding Proteins

FKBPs facilitate the termination of spontaneous Ca2+ release in wild-type RyR2 but not CPVT mutant RyR2

2016 ◽  
Vol 473 (14) ◽  
pp. 2049-2060 ◽  
Author(s):  
Joe Z. Zhang ◽  
Helen M.M. Waddell ◽  
Ella Wu ◽  
Jhanvi Dholakia ◽  
Chidinma A. Okolo ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Binding Proteins ◽  
Wild Type ◽  
Fk506 Binding Proteins ◽  
Cardiac Ryanodine Receptor

We show that the magnitude of Ca2+ release through the cardiac ryanodine receptor (RyR2) is controlled by the presence of FK506-binding proteins but that this regulation is lost when arrhythmogenic RyR2 mutations are present.

scholarly journals Mineralocorticoid Modulation of Cardiac Ryanodine Receptor Activity Is Associated With Downregulation of FK506-Binding Proteins

Circulation ◽  
2009 ◽  
Vol 119 (16) ◽  
pp. 2179-2187 ◽  
Author(s):  
Ana María Gómez ◽  
Angélica Rueda ◽  
Yannis Sainte-Marie ◽  
Laetitia Pereira ◽  
Spyros Zissimopoulos ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Binding Proteins ◽  
Receptor Activity ◽  
Fk506 Binding Proteins ◽  
Cardiac Ryanodine Receptor

scholarly journals Disparities in the association of the ryanodine receptor and the FK506-binding proteins in mammalian heart

2012 ◽  
Vol 125 (7) ◽  
pp. 1759-1769 ◽  
Author(s):  
S. Zissimopoulos ◽  
S. Seifan ◽  
C. Maxwell ◽  
A. J. Williams ◽  
F. A. Lai
Keyword(s):  
Ryanodine Receptor ◽  
Binding Proteins ◽  
Mammalian Heart ◽  
Fk506 Binding Proteins

scholarly journals Nitric Oxide-induced Activation of the Type 1 Ryanodine Receptor Is Critical for Epileptic Seizure-induced Neuronal Cell Death

EBioMedicine ◽  
2016 ◽  
Vol 11 ◽  
pp. 253-261 ◽  
Author(s):  
Yoshinori Mikami ◽  
Kazunori Kanemaru ◽  
Yohei Okubo ◽  
Takuya Nakaune ◽  
Junji Suzuki ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Cell Death ◽  
Ryanodine Receptor ◽  
Epileptic Seizure ◽  
Neuronal Cell Death ◽  
Neuronal Cell

scholarly journals Inhibition of FK506 Binding Proteins Reduces  -Synuclein Aggregation and Parkinson's Disease-Like Pathology

2010 ◽  
Vol 30 (7) ◽  
pp. 2454-2463 ◽  
Author(s):  
M. Gerard ◽  
A. Deleersnijder ◽  
V. Daniels ◽  
S. Schreurs ◽  
S. Munck ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Binding Proteins ◽  
Fk506 Binding Proteins

scholarly journals Recombinant Protein Truncation Strategy for Inducing Bactericidal Antibodies to the Macrophage Infectivity Potentiator Protein of Neisseria meningitidis and Circumventing Potential Cross-Reactivity with Human FK506-Binding Proteins

2014 ◽  
Vol 83 (2) ◽  
pp. 730-742 ◽  
Author(s):  
Magdalena K. Bielecka ◽  
Nathalie Devos ◽  
Mélanie Gilbert ◽  
Miao-Chiu Hung ◽  
Vincent Weynants ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Bactericidal Activity ◽  
Binding Proteins ◽  
Leader Peptide ◽  
Type I ◽  
Globular Domain ◽  
His Tag ◽  
Macrophage Infectivity Potentiator ◽  
Fk506 Binding Proteins ◽  
Macrophage Infectivity

A recombinant macrophage infectivity potentiator (rMIP) protein ofNeisseria meningitidisinduces significant serum bactericidal antibody production in mice and is a candidate meningococcal vaccine antigen. However, bioinformatics analysis of MIP showed some amino acid sequence similarity to human FK506-binding proteins (FKBPs) in residues 166 to 252 located in the globular domain of the protein. To circumvent the potential concern over generating antibodies that could recognize human proteins, we immunized mice with recombinant truncated type I rMIP proteins that lacked the globular domain and the signal leader peptide (LP) signal sequence (amino acids 1 to 22) and contained the His purification tag at either the N or C terminus (C-term). The immunogenicity of truncated rMIP proteins was compared to that of full (i.e., full-length) rMIP proteins (containing the globular domain) with either an N- or C-terminal His tag and with or without the LP sequence. By comparing the functional murine antibody responses to these various constructs, we determined that C-term His truncated rMIP (−LP) delivered in liposomes induced high levels of antibodies that bound to the surface of wild-type but not Δmipmutant meningococci and showed bactericidal activity against homologous type I MIP (median titers of 128 to 256) and heterologous type II and III (median titers of 256 to 512) strains, thereby providing at least 82% serogroup B strain coverage. In contrast, in constructs lacking the LP, placement of the His tag at the N terminus appeared to abrogate bactericidal activity. The strategy used in this study would obviate any potential concerns regarding the use of MIP antigens for inclusion in bacterial vaccines.

scholarly journals The 3-O-sulfation of heparan sulfate modulates protein binding and lyase degradation

2021 ◽  
Vol 118 (3) ◽  
pp. e2012935118
Author(s):  
Pradeep Chopra ◽  
Apoorva Joshi ◽  
Jiandong Wu ◽  
Weigang Lu ◽  
Tejabhiram Yadavalli ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Binding Proteins ◽  
Factor Xa ◽  
Tissue Expression ◽  
Cell Entry ◽  
Synthetic Approach ◽  
Array Technology ◽  
Wide Range ◽  
Simplex Virus

Humans express seven heparan sulfate (HS) 3-O-sulfotransferases that differ in substrate specificity and tissue expression. Although genetic studies have indicated that 3-O-sulfated HS modulates many biological processes, ligand requirements for proteins engaging with HS modified by 3-O-sulfate (3-OS) have been difficult to determine. In particular, the context in which the 3-OS group needs to be presented for binding is largely unknown. We describe herein a modular synthetic approach that can provide structurally diverse HS oligosaccharides with and without 3-OS. The methodology was employed to prepare 27 hexasaccharides that were printed as a glycan microarray to examine ligand requirements of a wide range of HS-binding proteins. The binding selectivity of antithrombin-III (AT-III) compared well with anti-Factor Xa activity supporting robustness of the array technology. Many of the other examined HS-binding proteins required an IdoA2S-GlcNS3S6S sequon for binding but exhibited variable dependence for the 2-OS and 6-OS moieties, and a GlcA or IdoA2S residue neighboring the central GlcNS3S. The HS oligosaccharides were also examined as inhibitors of cell entry by herpes simplex virus type 1, which, surprisingly, showed a lack of dependence of 3-OS, indicating that, instead of glycoprotein D (gD), they competitively bind to gB and gC. The compounds were also used to examine substrate specificities of heparin lyases, which are enzymes used for depolymerization of HS/heparin for sequence determination and production of therapeutic heparins. It was found that cleavage by lyase II is influenced by 3-OS, while digestion by lyase I is only affected by 2-OS. Lyase III exhibited sensitivity to both 3-OS and 2-OS.

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